(data stored in ACNUC30630 zone)

HOGENOM: CODIP1_1_PE1004

ID   CODIP1_1_PE1004                      STANDARD;      PRT;   481 AA.
AC   CODIP1_1_PE1004; Q6NHS9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP synthase subunit beta; EC=3.6.3 14;AltName: Full=ATP
DE   synthase F1 sector subunit beta;AltName: Full=F-ATPase subunit beta;
DE   (CODIP1_1.PE1004).
GN   Name=atpD; OrderedLocusNames=DIP1052;
OS   CORYNEBACTERIUM DIPHTHERIAE NCTC 13129.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CODIP1_1.PE1004.
CC       Corynebacterium diphtheriae NCTC 13129, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ATPB_CORDI
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The catalytic sites are hosted
CC       primarily by the beta subunits (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC   -!- GENE_FAMILY: HOG000009605 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6NHS9; -.
DR   EMBL; BX248356; CAE49572.1; -; Genomic_DNA.
DR   RefSeq; NP_939413.1; NC_002935.2.
DR   ProteinModelPortal; Q6NHS9; -.
DR   SMR; Q6NHS9; 17-478.
DR   GeneID; 2650818; -.
DR   GenomeReviews; BX248353_GR; DIP1052.
DR   KEGG; cdi:DIP1052; -.
DR   NMPDR; fig|257309.1.peg.1004; -.
DR   OMA; RDGEQWG; -.
DR   ProtClustDB; PRK09280; -.
DR   BioCyc; CDIP257309:DIP1052-MON; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1; -.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR005722; ATPase_F1-cplx_bsu.
DR   InterPro; IPR018118; ATPase_F1/A1-cplx_a/bsu_N.
DR   InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR   InterPro; IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1_bsu/V1_C.
DR   Gene3D; G3DSA:1.10.1140.10; G3DSA:1.10.1140.10; 1.
DR   PANTHER; PTHR15184:SF8; ATPase_F1_b; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; ATPase_a/b_C; 1.
DR   SUPFAM; SSF50615; ATPase_a/b_N; 1.
DR   TIGRFAMs; TIGR01039; AtpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR   HOGENOMDNA; CODIP1_1.PE1004; -.
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome;
KW   Hydrogen ion transport; Hydrolase; Ion transport; Membrane;
KW   Nucleotide-binding; Transport.
SQ   SEQUENCE   481 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTTALEEQNT QQASVAGRVV RVIGPVVDVE FPRGELPALY NALTVEVTLE AVAKTITLEV
     AQHLGDNLVR AVSMAPTDGL VRGAVVTDSG KPISVPVGDV VKGHVFNALG DCLDEPGLGR
     DGEQWGIHRD PPPFDQLEGK TEILETGIKV IDLLTPYVKG GKIGLFGGAG VGKTVLIQEM
     ITRIAREFSG TSVFAGVGER TREGTDLFLE MEEMGVLQDT ALVFGQMDEP PGVRMRVALS
     GLTMAEYFRD VQHQDVLLFI DNIFRFTQAG SEVSTLLGRM PSAVGYQPTL ADEMGVLQER
     ITSIKGKSIT SLQAVYVPAD DYTDPAPATT FAHLDATTEL DRAIASKGIY PAVNPLTSTS
     RILEPGIVGE RHYAVAQRVI NILQKNKELQ DIIAILGMDE LSEEDKITVQ RARRLERFLG
     QNFFVAEKFT GIPGSYVPLA HTIDAFERIC NGDFDHYPEQ AFNGLGGLDD VEAAYKKMTE
     K
//

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